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J. Biol. Chem., Vol. 276, Issue 19, 16193-16200, May 11, 2001
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From the Laboratory of Immune Cell Biology, Center for Cancer
Research, NCI, National Institutes of Health,
Bethesda, Maryland 20892-1152
Degradation of proteins from the endoplasmic
reticulum is fundamental to quality control within the secretory
pathway, serves as a way of regulating levels of crucial proteins, and
is utilized by viruses to enhance pathogenesis. In yeast two
ubiquitin-conjugating enzymes (E2s), UBC6p and UBC7p are implicated in
this process. We now report the characterization of murine homologs of
these E2s. MmUBC6 is an integral membrane protein that is anchored via its hydrophobic C-terminal tail to the endoplasmic reticulum. MmUBC7,
which is not an integral membrane protein, shows significant endoplasmic reticulum colocalization with MmUBC6. Overexpression of
catalytically inactive MmUBC7 significantly delayed degradation from
the endoplasmic reticulum of two T cell antigen receptor subunits, The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF 296656, AF 296657, and AF 296658.
Endoplasmic Reticulum (ER)-associated
Degradation of T Cell Receptor Subunits
INVOLVEMENT OF ER-ASSOCIATED UBIQUITIN-CONJUGATING ENZYMES
(E2s)*
and CD3-
, and suggests a role for the ubiquitin
conjugating system at the initiation of retrograde movement from the
endoplasmic reticulum. These findings also implicate, for the first
time, a specific E2 in degradation from the endoplasmic reticulum in mammalian cells.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. E-mail:
amw@nih.gov.
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